S-layer-streptavidin fusion proteins as template for nanopatterned molecular arrays
Open Access
- 4 November 2002
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 99 (23), 14646-14651
- https://doi.org/10.1073/pnas.232299399
Abstract
Biomolecular self-assembly can be used as a powerful tool for nanoscale engineering. In this paper, we describe the development of building blocks for nanobiotechnology, which are based on the fusion of streptavidin to a crystalline bacterial cell surface layer (S-layer) protein with the inherent ability to self-assemble into a monomolecular protein lattice. The fusion proteins and streptavidin were produced independently in Escherichia coli, isolated, and mixed to refold and purify heterotetramers of 1:3 stoichiometry. Self-assembled chimeric S-layers could be formed in suspension, on liposomes, on silicon wafers, and on accessory cell wall polymer containing cell wall fragments. The two-dimensional protein crystals displayed streptavidin in defined repetitive spacing, and they were capable of binding d-biotin and biotinylated proteins. Therefore, the chimeric S-layer can be used as a self-assembling nanopatterned molecular affinity matrix to arrange biotinylated compounds on a surface. In addition, it has application potential as a functional coat of liposomes.Keywords
This publication has 25 references indexed in Scilit:
- Characterization and use of crystalline bacterial cell surface layersProgress in Surface Science, 2001
- S-layer proteins as basic building blocks in a biomolecular construction kitNanotechnology, 2000
- S-Layer ProteinsJournal of Bacteriology, 2000
- The application of bacterial S-layers in molecular nanotechnologyTrends in Biotechnology, 1999
- Structural Research on Surface Layers: A Focus on Stability, Surface Layer Homology Domains, and Surface Layer–Cell Wall InteractionsJournal of Structural Biology, 1998
- Streptavidins with intersubunit crosslinks have enhanced stabilityNature Biotechnology, 1996
- Engineered Chimeric Streptavidin Tetramers as Novel Tools for Bioseparations and Drug DeliveryNature Biotechnology, 1995
- One-step affinity purification of bacterially produced proteins by means of the “Strep tag” and immobilized recombinant core streptavidinJournal of Chromatography A, 1994
- Two-dimensional crystals of streptavidin on biotinylated lipid layers and their interactions with biotinylated macromoleculesBiophysical Journal, 1991
- Paracrystalline Cell Wall Surface Layers of Different Bacillus stearothermophilus StrainsInternational Journal of Systematic and Evolutionary Microbiology, 1984